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glcD glcD acoL acoL glpD glpD thiO thiO pdhD pdhD murB murB coaBC coaBC yoaI yoaI lpdV lpdV sdhA sdhA etfB etfB
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query proteins and first shell of interactors
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second shell of interactors
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glcDGlycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. (470 aa)
acoLAcetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (458 aa)
glpDGlycerol-3-phosphate oxidase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (555 aa)
thiOFAD-dependent glycine oxidase; Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N- methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine interm [...] (369 aa)
pdhDDihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa)
murBUDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation. (303 aa)
coaBCCoenzyme A biosynthesis bifunctional protein CoaBC; Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. (406 aa)
yoaIPutative 4-hydroxyphenylacetate-3-hydroxylase; Catalyzes the hydroxylation of 4-hydroxyphenylacetic acid (4HPA), leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA). (483 aa)
lpdVBranched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (474 aa)
sdhASuccinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (586 aa)
etfBElectron transfer flavoprotein (beta subunit); The electron transfer flavoprotein serves as a specific electron acceptor for other dehydrogenases. It transfers the electrons to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (By similarity). (257 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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